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Gene Review

NARS  -  asparaginyl-tRNA synthetase

Homo sapiens

Synonyms: ASNRS, AsnRS, Asparagine--tRNA ligase, cytoplasmic, Asparaginyl-tRNA synthetase, NARS1
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Disease relevance of NARS


High impact information on NARS


Biological context of NARS

  • A bacterial extract containing the fusion protein catalyzed the aminoacylation reaction of S.cerevisiae tRNA with [14C]asparagine at a 20-fold efficiency level above the control value confirming that this cDNA encodes a human AsnRS [1].
  • Isolation and characterization of interspecific heat-resistant hybrids between a temperature-sensitive chinese hamster cell asparaginyl-tRNA synthetase mutant and normal human leukocytes: assignment of human asnS gene to chromosome 18 [9].
  • While the mechanism by which asparaginyl-tRNA synthetase affects cell-cycle progression has not been elucidated, it can be shown that it is not mediated through alteration in overall levels of protein synthesis [10].
  • Drug resistance in lymphoblastic and myeloblastic leukemia cells is poorly understood, with several lines of evidence suggesting that resistance can be correlated with upregulation of human asparagine synthetase (hASNS) expression, although this hypothesis is controversial [3].
  • Recombinant B. malayi AsnRS was used to perform cellular function assays--for example, chemotaxis and kinase activation assays.Results [11].

Anatomical context of NARS


Associations of NARS with chemical compounds

  • In other bacteria, particularly those that lack AsnRS, AspRS is nondiscriminating (ND-AspRS) and generates both Asp-tRNA(Asp) and the noncanonical, misacylated Asp-tRNA(Asn); this misacylated tRNA is subsequently repaired by the glutamine-dependent Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase (Asp/Glu-Adt) [13].
  • Analogs of one of these classes of inhibitors, the long side-chain variolins, cannot bind to the adenosyl pocket of the closed conformation of AsnRS due to steric clashes, though the short side-chain variolins identified by SLIDE apparently bind isosterically with adenosine [14].
  • In the absence of tRNA, AsnRS synthesizes diadenosine triphosphate, a potent regulator of cell growth in other eukaryotes [4].
  • The anomalous dispersion of a uranium derivative of asparaginyl-tRNA synthetase (hexagonal, a = 124.4 A, c = 123.4 A) has been measured at three wavelengths near the M(V) edge using beamline ID1 of the ESRF [15].
  • [3H]Asparagine was incorporated into protein by mitochondria of the Chinese hamster ovary (CHO) cell line Asn-7, which has a temperature-sensitive cytosolic asparaginyl-tRNA synthetase, either in the presence of cycloheximide or at a nonpermissive temperature [16].

Regulatory relationships of NARS

  • In corroboration with these results it was shown that a different temperature-sensitive asparaginyl-tRNA synthetase mutant isolated in another laboratory was blocked in S phase in a manner similar to that of ts24 [10].

Other interactions of NARS

  • The relative level of AsnRS transcribed in adult female B. malayi was compared to the levels of a low abundance and medium abundance AARS by quantitative real-time RT-PCR [4].
  • Mutants having low activity for MetRS, AsnRS, or GlnRS contained aaRSs that were inactivated much more rapidly upon heating than those from wild-type cells [17].
  • Under conditions of limited asparaginyl-tRNA synthetase activity in the mutant, there is a 2- to 3-fold increase in the level of asparagine synthetase activity [5].
  • A temperature-sensitive mutation in asparaginyl-tRNA synthetase causes cell-cycle arrest in early S phase [10].
  • The simulations are analyzed to determine the interactions that Asn is able to make in the binding pocket, and which sequence differences between AspRS and the highly homologous AsnRS are important for modifying the amino acid specificity [18].

Analytical, diagnostic and therapeutic context of NARS


  1. Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen. Beaulande, M., Tarbouriech, N., Härtlein, M. Nucleic Acids Res. (1998) [Pubmed]
  2. Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells. Howard, O.M., Dong, H.F., Yang, D., Raben, N., Nagaraju, K., Rosen, A., Casciola-Rosen, L., Härtlein, M., Kron, M., Yang, D., Yiadom, K., Dwivedi, S., Plotz, P.H., Oppenheim, J.J. J. Exp. Med. (2002) [Pubmed]
  3. An inhibitor of human asparagine synthetase suppresses proliferation of an L-asparaginase-resistant leukemia cell line. Gutierrez, J.A., Pan, Y.X., Koroniak, L., Hiratake, J., Kilberg, M.S., Richards, N.G. Chem. Biol. (2006) [Pubmed]
  4. Expression, localization and alternative function of cytoplasmic asparaginyl-tRNA synthetase in Brugia malayi. Kron, M., Petridis, M., Milev, Y., Leykam, J., Härtlein, M. Mol. Biochem. Parasitol. (2003) [Pubmed]
  5. A role for asparaginyl-tRNA in the regulation of asparagine synthetase in a mammalian cell line. Arfin, S.M., Simpson, D.R., Chiang, C.S., Andrulis, I.L., Hatfield, G.W. Proc. Natl. Acad. Sci. U.S.A. (1977) [Pubmed]
  6. Efficient procedure for transferring specific human genes into Chinese hamster cell mutants: interspecific transfer of the human genes encoding leucyl- and asparaginyl-tRNA synthetases. Cirullo, R.E., Dana, S., Wasmuth, J.J. Mol. Cell. Biol. (1983) [Pubmed]
  7. Evolutionary divergence of the archaeal aspartyl-tRNA synthetases into discriminating and nondiscriminating forms. Tumbula-Hansen, D., Feng, L., Toogood, H., Stetter, K.O., Söll, D. J. Biol. Chem. (2002) [Pubmed]
  8. Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family. Shiba, K., Motegi, H., Yoshida, M., Noda, T. Nucleic Acids Res. (1998) [Pubmed]
  9. Isolation and characterization of interspecific heat-resistant hybrids between a temperature-sensitive chinese hamster cell asparaginyl-tRNA synthetase mutant and normal human leukocytes: assignment of human asnS gene to chromosome 18. Cirullo, R.E., Arredondo-Vega, F.X., Smith, M., Wasmuth, J.J. Somatic Cell Genet. (1983) [Pubmed]
  10. A temperature-sensitive mutation in asparaginyl-tRNA synthetase causes cell-cycle arrest in early S phase. Diamond, G., Cedar, H., Marcus, M. Exp. Cell Res. (1989) [Pubmed]
  11. Brugia malayi Asparaginyl-Transfer RNA Synthetase Induces Chemotaxis of Human Leukocytes and Activates G-Protein-Coupled Receptors CXCR1 and CXCR2. Ramirez, B.L., Howard, O.M., Dong, H.F., Edamatsu, T., Gao, P., Hartlein, M., Kron, M. J. Infect. Dis. (2006) [Pubmed]
  12. Do tissue levels of autoantigenic aminoacyl-tRNA synthetase predict clinical disease? Kron, M.A., Petridis, M., Haertlein, M., Libranda-Ramirez, B., Scaffidi, L.E. Med. Hypotheses (2005) [Pubmed]
  13. The nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori: anticodon-binding domain mutations that impact tRNA specificity and heterologous toxicity. Chuawong, P., Hendrickson, T.L. Biochemistry (2006) [Pubmed]
  14. Discovering New Classes of Brugia malayi Asparaginyl-tRNA Synthetase Inhibitors and Relating Specificity to Conformational Change. Sukuru, S.C., Crepin, T., Milev, Y., Marsh, L.C., Hill, J.B., Anderson, R.J., Morris, J.C., Rohatgi, A., O'mahony, G., Grøtli, M., Danel, F., Page, M.G., Härtlein, M., Cusack, S., Kron, M.A., Kuhn, L.A. J. Comput. Aided Mol. Des. (2006) [Pubmed]
  15. Feasibility and review of anomalous X-ray diffraction at long wavelengths in materials research and protein crystallography. Kahn, R., Carpentier, P., Berthet-Colominas, C., Capitan, M., Chesne, M.L., Fanchon, E., Lequien, S., Thiaudière, D., Vicat, J., Zielinski, P., Stuhrmann, H. Journal of synchrotron radiation. (2000) [Pubmed]
  16. Biochemical and genetic approaches to the study of mammalian mitochondrial tRNAs. Aujame, L., Yatscoff, R.W., Freeman, K.B. Can. J. Biochem. (1978) [Pubmed]
  17. Evidence for structural gene alterations affecting aminoacyl-tRNA synthetases in CHO cell mutants and revertants. Thompson, L.H., Lofgren, D.J., Adair, G.M. Somatic Cell Genet. (1978) [Pubmed]
  18. Specific amino acid recognition by aspartyl-tRNA synthetase studied by free energy simulations. Archontis, G., Simonson, T., Moras, D., Karplus, M. J. Mol. Biol. (1998) [Pubmed]
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